This project will continue to be concerned with studies of the structure and function of hemoglobin. The influence of membrane proteins on the oxygen equilibrium of hemoglobin, and the interactions of membrane proteins, 2,3-DPG and hemoglobin are being studied. The kinetics of the reactions of hemoglobin with ligands using stopped flow techniques are being investigated by a new method devised in this laboratory. Studies of abnormal hemoglobins include an 'unstable' hemoglobin and the completion of studies of the interactions of a patient with HbC Harlem in comparison with Hb S. The proportions of glycohemoglobins in experimental anemias with diabetes are being investigated to provide a better system for studies of the correlation of disordered carbohydrate metabolism, glycohemoglobins and vascular disease. BIBLIOGRAPHIC REFERENCES: Sharma, V.S., Ranney, H.M., Geiber, J.R. and Traylor, T.G.: A new method for the determination of ligand dissociation rate constant of carboxyhemoglobin. Biochem. Biophys. Res. Comm. 66:1301-1306, 1975. Sharma, V.S., Schmidt, M.R., and Ranney, H.M.: Dissociation of CO from Carboxyhemoglobin. (Abstract, presented at American Society of Biological Chemists Meeting, June 7, 1976. In Press, Fed. Proc.).